ID G8PE62_PEDCP Unreviewed; 825 AA.
AC G8PE62;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:AEV95547.1};
GN Name=clpC {ECO:0000313|EMBL:AEV95547.1};
GN OrderedLocusNames=PECL_1315 {ECO:0000313|EMBL:AEV95547.1};
OS Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC
OS 3811 / P06).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV95547.1, ECO:0000313|Proteomes:UP000005444};
RN [1] {ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Genome and plasmid sequences for the beer-spoilage organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV95547.1, ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RX PubMed=22328764; DOI=10.1128/JB.06759-11;
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Complete Genome Sequence of the Beer Spoilage Organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL J. Bacteriol. 194:1271-1272(2012).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP003137; AEV95547.1; -; Genomic_DNA.
DR RefSeq; WP_014215741.1; NC_016605.1.
DR AlphaFoldDB; G8PE62; -.
DR STRING; 701521.PECL_1315; -.
DR KEGG; pce:PECL_1315; -.
DR PATRIC; fig|701521.8.peg.1226; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000005444; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AEV95547.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AEV95547.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005444};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 425..460
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 151..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..448
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 153..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 91197 MW; 03BF94BDAD3785DD CRC64;
MDNLFTPSAK NVLMIAQEQA KKFKHPAVGT EHLLLALTIE QNGVAKSVLD QFNVQEVDVT
EEIESFTGYG NLTSRKNDYL PYSPKAKEIL SLAGDEAKQL KSSKIGTEHL LLALLQDDSI
LSSRILAALD ISVSDVQKVA LRKLGVNPAV RARQARQRQT NGGQSSATPT LDSVARDLTE
MAAEGQIDPV VGRSKEVRRV IQILSRRTKN NPVLIGEPGV GKTAIAEGLA QRIVDGDVPE
DMQNKRLMML EMGSLVAGTK YRGEFEDRLK KVIEEIRTDK GIILFIDELH TLIGAGGAEG
AIDASNILKP ALARGELQTI GATTLNEYQK YIESDAALER RFARVEVNEP TEDEAIQILK
GLRGKYEEHH HVEITDEAIV EAVKLSSRYI SDRYLPDKAI DLIDEAAAKI RIDGSEKPDS
KSKNEAKLAE LRQEKEDAID AQEFEKAATI REKEFKLAKK VEKQNNDSEK ADSKNEYDLV
ETAESVAEIV SDWTGVPLTH LEQAESDRLI NLEKTLHERV IGQDEAVSAV ARAIRRARSG
LKDPKRPIGS FMFLGPTGVG KTELAKTLAD VMFGSEDNMI RIDMSEYMER YSTSRLVGSA
PGYVGYDEGG QLTEQVRRKP YSVVLFDEVE KAHPDVFNLL LQVLDDGFLT DSKGRRVDFR
NTILIMTSNL GATALRDEKS VGFAAKNASE DYNAMSAKVR EILKQSFRPE FLNRIDETII
FHSLTKEELH SIVKLMAKDV ILRMSEQGIN TKLTPAAIDA VADAGFDPEF GARPIRRALQ
TDVEDKLSEL ILSGEATVGD DVTVGARNGK ITFKVSSVQK NKVNN
//